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. Author manuscript; available in PMC: 2017 Jul 1.
Published in final edited form as: Subcell Biochem. 2016;81:21–76. doi: 10.1007/978-94-024-0945-1_2

Fig. 2.6.

Fig. 2.6

Kinetic relationships between RDH and CRBP1-retinol. The top panel shows the Michaelis-Menten relationship (substrate-concentration dependent, saturable kinetics, initial velocity conditions) between holo-CRBP1 and the rate of retinal formation catalyzed by microsomes. The kinetic constants generated were independent of the ratio total CRBP1/retinol, indicating ability of CRBP1 to deliver retinol without diffusion. The bottom panel shows the impact of mutating external residues of CRBP1 on kinetics of retinal formation using microsomes as source of RDH. The sensitivity of the kinetics to changes in one external CRBP amino acid residue, without affecting affinity for retinol, corroborates an interaction between RDH and CRBP1